α-synuclein aggregation is involved in the pathogenesis of Parkinson’s disease. The prevailing hypothesis on amyloid toxicity involves membrane disruption by oligomeric species. However, isolated α-synuclein oligomers only transiently disrupt the membrane and vesicles remain intact. We studied synuclein aggregation in giant unilamellar vesicles and observed dramatic membrane disintegration and incorporation of lipids into fibrillar aggregates. Aggregation of α-synuclein in the presence of calcein filled vesicles shows synchronous leakage of dye with fibrillization. The evolving picture suggests that fibrillization and membrane disintegration during the aggregation process may be more relevant for toxicity than permeabilization by stable oligomeric species.
|Journal||European biophysics journal|
|Issue number||Suppl. 1|
|Publication status||Published - 2013|
|Event||9th European Biophysics Congress, EBSA 2013 - Lisbon, Portugal|
Duration: 13 Jul 2013 → 17 Jul 2013
Conference number: 9